PURIFICATION AND PROPERTIES OF A FIBRIN CROSS-LINKING TRANSAMIDASE FROM RABBIT LIVER

Rabbit liver is a rich source of fibrin cross-linking enzyme. Pooled rabbit livers, previously perfused until free of blood, were homogenized in 0.25 [image] sucrose and subjected to high-speed centrifugation. The fibrin cross-linking enzyme was purified from the high-speed supernatant by isoelectric precipitation and ion-exchange chromatography. Over-all purification was 100-fold. The enzyme is Ca2+ dependent, heat labile, and is inhibited by p-mercuribenzoate, iodoacetamide, and some primary amines. The rabbit liver enzyme readily incorporates [14C]-glycine ethyl ester into casein, thus resembling in this and other properties both the guinea pig liver transglutaminase and the plasma clot-stabilizing enzyme.